{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,20]],"date-time":"2025-10-20T10:00:30Z","timestamp":1760954430693},"reference-count":29,"publisher":"American Society for Microbiology","issue":"1","license":[{"start":{"date-parts":[[2001,1,1]],"date-time":"2001-01-01T00:00:00Z","timestamp":978307200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2001,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            HrcA, a negative control repressor for chaperone expression from the obligate thermophile\n            <jats:italic>Bacillus thermoglucosidasius<\/jats:italic>\n            KP1006, was purified in a His-tagged form in the presence of 6 M urea but hardly renatured to an intact state due to extreme insolubility. Renaturation trials revealed that the addition of DNA to purified\n            <jats:italic>B. thermoglucosidasius<\/jats:italic>\n            HrcA can result in solubilization of HrcA free from the denaturing agent urea. Results from band shift and light scattering assays provided three new findings: (i) any species of DNA can serve to solubilize\n            <jats:italic>B. thermoglucosidasius<\/jats:italic>\n            HrcA, but DNA containing the CIRCE (controlling inverted repeat of chaperone expression) element is far more effective than other nonspecific DNA; (ii)\n            <jats:italic>B. thermoglucosidasius<\/jats:italic>\n            HrcA renatured with nonspecific DNA bound the CIRCE element in the molecular ratio of 2.6:1; and (iii)\n            <jats:italic>B. thermoglucosidasius<\/jats:italic>\n            HrcA binding to the CIRCE element was stable at below 50\u00b0C whereas the complex was rapidly denatured at 70\u00b0C, suggesting that the breakdown of HrcA is induced by heat stress and HrcA may act as a thermosensor to affect the expression of heat shock regulatory genes. These results will help to determine the nature of HrcA protein molecules.\n          <\/jats:p>","DOI":"10.1128\/jb.183.1.155-161.2001","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T10:01:09Z","timestamp":1027764069000},"page":"155-161","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":19,"title":["Renaturation of\n            <i>Bacillus thermoglucosidasius<\/i>\n            HrcA Repressor by DNA and Thermostability of the HrcA-DNA Complex In Vitro"],"prefix":"10.1128","volume":"183","author":[{"given":"Kunihiko","family":"Watanabe","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Department of Applied Biochemistry, Kyoto Prefectural University, Shimogamo, Sakyo, Kyoto 606-8522, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Takeshi","family":"Yamamoto","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Department of Applied Biochemistry, Kyoto Prefectural University, Shimogamo, Sakyo, Kyoto 606-8522, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yuzuru","family":"Suzuki","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Department of Applied Biochemistry, Kyoto Prefectural University, Shimogamo, Sakyo, Kyoto 606-8522, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_1_2_2","doi-asserted-by":"crossref","first-page":"1387","DOI":"10.1099\/00207713-49-4-1387","article-title":"A protein-based phylogenetic tree for gram-positive bacteria derived from hrcA, a unique heat-shock regulatory gene","volume":"49","author":"Ahmad S.","year":"1999","unstructured":"Ahmad S. 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